The synthetic peptide sequence is 641-672aa, KALLFSKGRVWRFDLKSQKVDPQSVIRVDKEF
Add 0.2 mL of distilled water, will yield a concentration of 500 µg/mL.
MMP9 (matrix metallopeptidase 9, GELB, CLG4B) is a matrix metalloproteinase, a family of zinc and calcium-dependent endopeptidases that degrade extracellular matrix proteins. MMP9 is secreted as a 92kDa zymogen and cleavage of pro-MMP9 results in the active enzyme with a molecular weight of 82kDa. MMP9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 is supplied by bone marrow-derived cells and contributes to skin carcinogenesis. Further, MMP9 degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Studies have shown that elevated MMP9 is associated with progression of idiopathic atrial fibrillation and aortic aneurysm.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: 92 kDa gelatinase; 92 kDa type IV collagenase; 92-kDa type IV collagenase; 92kD gelatinase; 92kD type IV collagenase; 92kDa gelatinase; 92kDa type IV collagenase; collagenase type IVB; Gel B; Gelatinase B; Gelatinase-B; GELB; matrix metallo protease; matrix metalloproteinase 9; matrix metalloproteinase 9 (gelatinase B 92-kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92-kDa type IV collagenase); Matrix metalloproteinase-9; Matrix metalloproteinase9; MMP; MMP-9; MMPs
Gene Aliases: AW743869; B/MMP9; Clg4b; MMP-9; Mmp9; pro-MMP-9